FMO DATABASE

FMODB ID: 6YLZZ

Calculation Name: 2ANE-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 2ANE

Chain ID: A

ChEMBL ID:

UniProt ID: P0A9M0

Base Structure: X-ray

Registration Date: 2023-09-20

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	110
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-860461.20888
FMO2-HF: Nuclear repulsion	817613.950058
FMO2-HF: Total energy	-42847.258822
FMO2-MP2: Total energy	-42971.064788

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:8:ARG)

Summations of interaction energy for fragment #1(A:8:ARG)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-57.731	-52.536	2.801	-3.649	-4.346	-0.024

Interaction energy analysis for fragmet #1(A:8:ARG)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 1 / q_Mulliken : 0.902 / q_NPA : 0.935

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	10	GLU	-1	-0.906	-0.957	3.798	-30.425	-28.293	-0.033	-1.071	-1.027	0.000
4	A	11	ILE	0	-0.076	-0.018	6.716	1.394	1.394	0.000	0.000	0.000	0.000
5	A	12	PRO	0	0.085	0.043	9.547	0.017	0.017	0.000	0.000	0.000	0.000
6	A	13	VAL	0	0.011	-0.002	11.910	-0.229	-0.229	0.000	0.000	0.000	0.000
7	A	14	LEU	0	0.017	0.006	14.157	0.752	0.752	0.000	0.000	0.000	0.000
8	A	15	PRO	0	-0.037	-0.007	17.470	-0.255	-0.255	0.000	0.000	0.000	0.000
9	A	16	LEU	0	-0.011	-0.015	19.296	0.529	0.529	0.000	0.000	0.000	0.000
10	A	17	ARG	1	0.849	0.905	21.399	9.465	9.465	0.000	0.000	0.000	0.000
11	A	18	ASP	-1	-0.842	-0.925	24.569	-9.754	-9.754	0.000	0.000	0.000	0.000
12	A	19	VAL	0	-0.025	0.008	22.825	0.206	0.206	0.000	0.000	0.000	0.000
13	A	20	VAL	0	0.008	0.003	19.521	-0.441	-0.441	0.000	0.000	0.000	0.000
14	A	21	VAL	0	0.020	0.014	18.398	0.343	0.343	0.000	0.000	0.000	0.000
15	A	22	TYR	0	-0.010	-0.023	17.426	-0.967	-0.967	0.000	0.000	0.000	0.000
16	A	23	PRO	0	-0.050	-0.033	14.609	0.207	0.207	0.000	0.000	0.000	0.000
17	A	24	HIS	0	0.038	0.006	17.082	0.656	0.656	0.000	0.000	0.000	0.000
18	A	25	MET	0	-0.054	0.028	20.007	0.439	0.439	0.000	0.000	0.000	0.000
19	A	26	VAL	0	0.044	0.023	20.904	-0.397	-0.397	0.000	0.000	0.000	0.000
20	A	27	ILE	0	-0.019	-0.015	22.143	0.401	0.401	0.000	0.000	0.000	0.000
21	A	28	PRO	0	-0.030	-0.017	23.905	-0.281	-0.281	0.000	0.000	0.000	0.000
22	A	29	LEU	0	0.004	0.002	20.878	0.138	0.138	0.000	0.000	0.000	0.000
23	A	30	PHE	0	-0.011	-0.013	25.350	0.138	0.138	0.000	0.000	0.000	0.000
24	A	31	VAL	0	0.008	0.002	23.167	-0.232	-0.232	0.000	0.000	0.000	0.000
25	A	32	GLY	0	0.062	0.029	26.405	0.204	0.204	0.000	0.000	0.000	0.000
26	A	33	ARG	1	0.899	0.956	25.850	10.347	10.347	0.000	0.000	0.000	0.000
27	A	34	GLU	-1	-0.860	-0.942	25.802	-9.842	-9.842	0.000	0.000	0.000	0.000
28	A	35	LYS	1	0.887	0.947	20.718	12.512	12.512	0.000	0.000	0.000	0.000
29	A	36	SER	0	0.016	-0.011	21.154	-0.532	-0.532	0.000	0.000	0.000	0.000
30	A	37	ILE	0	-0.022	-0.003	21.444	-0.340	-0.340	0.000	0.000	0.000	0.000
31	A	38	ARG	1	0.959	0.976	21.605	11.077	11.077	0.000	0.000	0.000	0.000
32	A	39	CYS	0	-0.060	-0.028	17.299	-0.512	-0.512	0.000	0.000	0.000	0.000
33	A	40	LEU	0	-0.012	-0.012	17.657	-0.529	-0.529	0.000	0.000	0.000	0.000
34	A	41	GLU	-1	-0.856	-0.931	19.373	-11.287	-11.287	0.000	0.000	0.000	0.000
35	A	42	ALA	0	0.062	0.042	16.254	-0.201	-0.201	0.000	0.000	0.000	0.000
36	A	43	ALA	0	-0.019	-0.007	15.082	-0.540	-0.540	0.000	0.000	0.000	0.000
37	A	44	MET	0	-0.085	-0.054	16.050	-0.342	-0.342	0.000	0.000	0.000	0.000
38	A	45	ASP	-1	-0.945	-0.945	18.812	-12.818	-12.818	0.000	0.000	0.000	0.000
39	A	46	HIS	0	-0.087	-0.045	10.379	-0.762	-0.762	0.000	0.000	0.000	0.000
40	A	47	ASP	-1	-0.877	-0.953	11.258	-19.883	-19.883	0.000	0.000	0.000	0.000
41	A	48	LYS	1	0.897	0.947	14.910	12.853	12.853	0.000	0.000	0.000	0.000
42	A	49	LYS	1	0.927	0.988	10.255	20.784	20.784	0.000	0.000	0.000	0.000
43	A	50	ILE	0	0.034	0.007	12.990	-0.360	-0.360	0.000	0.000	0.000	0.000
44	A	51	MET	0	-0.054	-0.012	9.303	-0.548	-0.548	0.000	0.000	0.000	0.000
45	A	52	LEU	0	0.003	0.007	12.285	0.591	0.591	0.000	0.000	0.000	0.000
46	A	53	VAL	0	-0.012	-0.014	13.241	-0.622	-0.622	0.000	0.000	0.000	0.000
47	A	54	ALA	0	0.012	0.018	15.878	0.621	0.621	0.000	0.000	0.000	0.000
48	A	55	GLN	0	0.015	-0.001	18.755	-0.685	-0.685	0.000	0.000	0.000	0.000
49	A	56	LYS	1	0.875	0.930	19.411	13.910	13.910	0.000	0.000	0.000	0.000
50	A	57	GLU	-1	-0.965	-0.971	23.275	-10.502	-10.502	0.000	0.000	0.000	0.000
51	A	58	ALA	0	-0.005	0.010	26.937	0.139	0.139	0.000	0.000	0.000	0.000
52	A	59	SER	0	-0.021	-0.015	25.083	0.151	0.151	0.000	0.000	0.000	0.000
53	A	60	THR	0	0.028	0.009	27.049	0.116	0.116	0.000	0.000	0.000	0.000
54	A	61	ASP	-1	-0.845	-0.924	26.721	-9.961	-9.961	0.000	0.000	0.000	0.000
55	A	62	GLU	-1	-1.018	-1.014	26.018	-11.067	-11.067	0.000	0.000	0.000	0.000
56	A	63	PRO	0	-0.035	0.000	22.027	-0.019	-0.019	0.000	0.000	0.000	0.000
57	A	64	GLY	0	0.118	0.046	22.314	-0.158	-0.158	0.000	0.000	0.000	0.000
58	A	65	VAL	0	0.020	-0.020	16.695	-0.182	-0.182	0.000	0.000	0.000	0.000
59	A	66	ASN	0	-0.055	-0.028	17.849	-0.896	-0.896	0.000	0.000	0.000	0.000
60	A	67	ASP	-1	-0.819	-0.899	19.788	-11.651	-11.651	0.000	0.000	0.000	0.000
61	A	68	LEU	0	-0.029	-0.003	16.411	0.333	0.333	0.000	0.000	0.000	0.000
62	A	69	PHE	0	-0.035	-0.020	16.145	-0.325	-0.325	0.000	0.000	0.000	0.000
63	A	70	THR	0	0.022	0.009	12.319	-0.208	-0.208	0.000	0.000	0.000	0.000
64	A	71	VAL	0	-0.025	-0.014	11.334	-1.793	-1.793	0.000	0.000	0.000	0.000
65	A	72	GLY	0	0.046	0.010	11.508	1.106	1.106	0.000	0.000	0.000	0.000
66	A	73	THR	0	-0.097	-0.081	11.974	-0.979	-0.979	0.000	0.000	0.000	0.000
67	A	74	VAL	0	0.000	0.015	8.042	0.374	0.374	0.000	0.000	0.000	0.000
68	A	75	ALA	0	0.015	-0.007	11.420	0.534	0.534	0.000	0.000	0.000	0.000
69	A	76	SER	0	0.016	0.020	14.418	-0.590	-0.590	0.000	0.000	0.000	0.000
70	A	77	ILE	0	0.008	-0.006	16.435	0.688	0.688	0.000	0.000	0.000	0.000
71	A	78	LEU	0	-0.022	-0.017	19.372	0.102	0.102	0.000	0.000	0.000	0.000
72	A	79	GLN	0	-0.071	-0.040	22.325	0.552	0.552	0.000	0.000	0.000	0.000
73	A	80	MET	0	0.041	0.026	23.527	-0.303	-0.303	0.000	0.000	0.000	0.000
74	A	81	LEU	0	-0.022	0.002	25.608	0.167	0.167	0.000	0.000	0.000	0.000
75	A	82	LYS	1	0.883	0.932	27.147	10.028	10.028	0.000	0.000	0.000	0.000
76	A	83	LEU	0	-0.032	-0.008	30.210	0.244	0.244	0.000	0.000	0.000	0.000
77	A	84	PRO	0	-0.007	-0.014	33.565	-0.082	-0.082	0.000	0.000	0.000	0.000
78	A	85	ASP	-1	-0.898	-0.967	34.452	-8.256	-8.256	0.000	0.000	0.000	0.000
79	A	86	GLY	0	0.024	0.029	32.647	0.007	0.007	0.000	0.000	0.000	0.000
80	A	87	THR	0	-0.055	0.004	30.532	-0.412	-0.412	0.000	0.000	0.000	0.000
81	A	88	VAL	0	0.019	-0.009	25.235	0.009	0.009	0.000	0.000	0.000	0.000
82	A	89	LYS	1	0.937	0.979	27.836	8.829	8.829	0.000	0.000	0.000	0.000
83	A	90	VAL	0	0.009	-0.001	21.619	-0.019	-0.019	0.000	0.000	0.000	0.000
84	A	91	LEU	0	-0.034	-0.004	24.108	0.056	0.056	0.000	0.000	0.000	0.000
85	A	92	VAL	0	0.003	0.002	18.795	-0.326	-0.326	0.000	0.000	0.000	0.000
86	A	93	GLU	-1	-0.885	-0.950	18.828	-12.478	-12.478	0.000	0.000	0.000	0.000
87	A	94	GLY	0	-0.003	0.002	16.183	-0.750	-0.750	0.000	0.000	0.000	0.000
88	A	95	LEU	0	-0.027	-0.011	12.813	0.186	0.186	0.000	0.000	0.000	0.000
89	A	96	GLN	0	0.009	-0.012	9.409	-0.593	-0.593	0.000	0.000	0.000	0.000
90	A	97	ARG	1	0.963	0.990	11.251	16.394	16.394	0.000	0.000	0.000	0.000
91	A	98	ALA	0	0.015	0.004	6.368	-1.146	-1.146	0.000	0.000	0.000	0.000
92	A	99	ARG	1	0.958	0.979	6.951	27.167	27.167	0.000	0.000	0.000	0.000
93	A	100	ILE	0	0.008	0.009	6.595	-3.209	-3.209	0.000	0.000	0.000	0.000
94	A	101	SER	0	-0.069	-0.029	5.071	0.963	0.963	0.000	0.000	0.000	0.000
95	A	102	ALA	0	0.004	-0.006	7.441	1.677	1.677	0.000	0.000	0.000	0.000
96	A	103	LEU	0	0.001	0.014	9.619	-0.886	-0.886	0.000	0.000	0.000	0.000
97	A	104	SER	0	-0.045	-0.020	12.336	0.681	0.681	0.000	0.000	0.000	0.000
98	A	105	ASP	-1	-0.780	-0.888	14.537	-13.689	-13.689	0.000	0.000	0.000	0.000
99	A	106	ASN	0	-0.064	-0.041	13.462	0.447	0.447	0.000	0.000	0.000	0.000
100	A	107	GLY	0	0.017	0.024	17.748	0.220	0.220	0.000	0.000	0.000	0.000
101	A	108	GLU	-1	-0.864	-0.927	19.892	-11.509	-11.509	0.000	0.000	0.000	0.000
102	A	109	HIS	0	-0.041	-0.052	15.066	0.676	0.676	0.000	0.000	0.000	0.000
103	A	110	PHE	0	-0.009	0.000	15.492	-0.493	-0.493	0.000	0.000	0.000	0.000
104	A	111	SER	0	-0.009	0.014	11.449	-0.471	-0.471	0.000	0.000	0.000	0.000
105	A	112	ALA	0	0.034	0.006	9.106	0.385	0.385	0.000	0.000	0.000	0.000
106	A	113	LYS	1	0.977	1.024	4.976	28.993	28.993	0.000	0.000	0.000	0.000
107	A	114	ALA	0	-0.008	-0.030	4.421	1.481	1.674	-0.001	-0.053	-0.139	0.000
108	A	115	GLU	-1	-0.933	-0.967	2.476	-55.751	-53.067	2.812	-2.586	-2.910	-0.023
109	A	116	TYR	0	0.008	0.003	3.383	4.345	4.531	0.023	0.061	-0.270	-0.001
110	A	117	LEU	0	-0.028	-0.004	6.076	-0.877	-0.877	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:8:ARG)